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Database: UniProt
Entry: B3F2H6_LEPBY
LinkDB: B3F2H6_LEPBY
Original site: B3F2H6_LEPBY 
ID   B3F2H6_LEPBY            Unreviewed;       494 AA.
AC   B3F2H6;
DT   22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE            EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN   Name=nifD {ECO:0000313|EMBL:ABU63067.1};
OS   Leptolyngbya boryana PCC 6306.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=272134 {ECO:0000313|EMBL:ABU63067.1};
RN   [1] {ECO:0000313|EMBL:ABU63067.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 6306 {ECO:0000313|EMBL:ABU63067.1};
RA   Menke S.M., Henson B.J., Barnum S.R.;
RT   "NifD: its Evolution and Phylogenetic Use in Cyanobacteria.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC       complex that catalyzes the key enzymatic reactions in nitrogen
CC       fixation. {ECO:0000256|ARBA:ARBA00002621}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC         ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC         phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=1.18.6.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000805,
CC         ECO:0000256|RuleBase:RU004022};
CC   -!- COFACTOR:
CC       Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC         Evidence={ECO:0000256|ARBA:ARBA00001969};
CC   -!- COFACTOR:
CC       Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC         Evidence={ECO:0000256|ARBA:ARBA00001919};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC       the iron protein (nitrogenase component 2).
CC       {ECO:0000256|ARBA:ARBA00011462}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC       {ECO:0000256|RuleBase:RU004021}.
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DR   EMBL; EF576854; ABU63067.1; -; Genomic_DNA.
DR   RefSeq; WP_017289030.1; NZ_KB731324.1.
DR   AlphaFoldDB; B3F2H6; -.
DR   SMR; B3F2H6; -.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd01976; Nitrogenase_MoFe_alpha; 1.
DR   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR010143; Nase_comp1_asu.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR005972; Nase_Mo-Fe_asu.
DR   NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR   NCBIfam; TIGR01282; nifD; 1.
DR   PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU004022};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004022}; Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW   ECO:0000256|RuleBase:RU004021};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU004022}.
FT   DOMAIN          70..480
FT                   /note="Nitrogenase/oxidoreductase component 1"
FT                   /evidence="ECO:0000259|Pfam:PF00148"
SQ   SEQUENCE   494 AA;  55423 MW;  F4E8DFD78FFE01DD CRC64;
     MTPPESVTLE ENAATAVDPK ELIKDVLEAY PEKGRKKREK HLNVYQEGKP DCGVKSNIKS
     LPGSMTTRGC AYAGSKGVVW GPIKDMIHIS HGPVGCGYYS WSGRRNYYIG TTGIDTFGTM
     QFTSDFQERD IVFGGDKKLA KLITELEELF PLNRGISIQS ECPIGLIGDD IEAVAKKSAK
     EINKAVVPVR CEGFRGVSQS LGHHIANDAV RDWIFPRTDK AKKDGTIDVD PTQYDVAIIG
     DYNIGGDAWS SRILLEEIGL RVVAQWSGDG TINELINTPT VKLNLVHCYR SMNYISRHME
     ETYGIPWLEY NFFGPTQIAK SLREIAAKFD ETIQAKAEEV IAKYQAQTDE VIAKFLPRLQ
     GKTVALMVGG LRPRHVVPAF YDLGMRLIGT GYEFGHNDDY KRTTHYIEDG TLIYDDVSAF
     EFEEFIKEMK PDLVASGIKE KYVFQKMALP FRQMHSWDYS GPYHGYDGFA IFARDMDMAL
     NSPTWSLIGA PWSK
//
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